Evidence mapPaperPMID 37993467Full record

ArticleNature communications2023

Orthosteric and allosteric modulation of human HCAR2 signaling complex.

Chunyou Mao, Mengru Gao, Shao-Kun Zang, Yanqing Zhu, Dan-Dan Shen, Li-Nan Chen, Liu Yang, Zhiwei Wang, Huibing Zhang, Wei-Wei Wang and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural Perspectives on Biased Allostery of GPCR Signaling.Handbook of experimental pharmacology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 6 institutions in 2 countries.

Chunyou Mao *Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, China. maochunyou@zju.edu.cn.ORCID 0000-0001-5349-8592
Mengru Gao *School of Medicine, Jiangnan University, Wuxi, 214122, China.
Shao-Kun Zang *Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, China.
Yanqing Zhu *Department of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, China.
Dan-Dan ShenDepartment of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, China.ORCID 0000-0001-8757-4602
Li-Nan ChenDepartment of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, China.
Liu YangSchool of Medicine, Jiangnan University, Wuxi, 214122, China.
Zhiwei WangSchool of Medicine, Jiangnan University, Wuxi, 214122, China.
Huibing ZhangLiangzhu Laboratory, Zhejiang University Medical Center, Hangzhou, 311121, China.ORCID 0000-0003-3025-0185
Wei-Wei WangLiangzhu Laboratory, Zhejiang University Medical Center, Hangzhou, 311121, China.
Qingya ShenLiangzhu Laboratory, Zhejiang University Medical Center, Hangzhou, 311121, China.ORCID 0000-0001-6602-7116
Yanhui LuSchool of Nursing, Peking University, 100191, Beijing, China. luyanhui@bjmu.edu.cn.
Xin MaSchool of Medicine, Jiangnan University, Wuxi, 214122, China. maxin@jiangnan.edu.cn.ORCID 0000-0001-8525-068X
Yan ZhangDepartment of Biophysics and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, China. zhang_yan@zju.edu.cn.ORCID 0000-0003-2189-0244
Jiangnan University · CNSir Run Run Shaw Hospital · CNZhejiang University · CNAllen Institute for Brain Science · USPeking University · CNZhejiang Chinese Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydroxycarboxylic acids are crucial metabolic intermediates involved in various physiological and pathological processes, some of which are recognized by specific hydroxycarboxylic acid receptors (HCARs). HCAR2 is one such receptor, activated by endogenous β-hydroxybutyrate (3-HB) and butyrate, and is the target for Niacin. Interest in HCAR2 has been driven by its potential as a therapeutic target in cardiovascular and neuroinflammatory diseases. However, the limited understanding of how ligands bind to this receptor has hindered the development of alternative drugs able to avoid the common flushing side-effects associated with Niacin therapy. Here, we present three high-resolution structures of HCAR2-Gi1 complexes bound to four different ligands, one potent synthetic agonist (MK-6892) bound alone, and the two structures bound to the allosteric agonist compound 9n in conjunction with either the endogenous ligand 3-HB or niacin. These structures coupled with our functional and computational analyses further our understanding of ligand recognition, allosteric modulation, and activation of HCAR2 and pave the way for the development of high-efficiency drugs with reduced side-effects.

Indexed as

NiacinReceptors, G-Protein-CoupledAllosteric RegulationAllosteric SiteHumansLigandsSignal TransductionLigandsNiacinReceptors, G-Protein-Coupled

Identifiers

PMID37993467
PMCPMC10665550
OpenAlexW4388904096

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.